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Search results

1000 results found for “osteoprotegerin”

Name

Description

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  • View Data Sheet

    Name :

    ORM2 Human

    Description:

    Orosomucoid 2 Human Recombinant

    Orosomucoid 2, Alpha-1-Acid Glycoprotein Type 2, OMD 2, AGP2, AGP-B, Type 2.

    Product # :

    PRO-1560

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    Description

    ORM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (19-201) and having a molecular mass of 24.3kDa.ORM2 is fused to a 25 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The ORM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      ORM2 is a significant acute phase plasma protein. ORM2 is highly expressed as a result of acute inflammation there for it is categorized as an acute-phase reactant.

    • Synonyms

      Orosomucoid 2, Alpha-1-Acid Glycoprotein Type 2, OMD 2, AGP2, AGP-B, Type 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMQIPLC ANLVPVPITN ATLDRITGKW FYIASAFRNE EYNKSVQEIQ ATFFYFTPNK TEDTIFLREY QTRQNQCFYN SSYLNVQREN GTVSRYEGGR EHVAHLLFLR DTKTLMFGSY LDDEKNWGLS FYADKPETTK EQLGEFYEAL DCLCIPRSDV MYTDWKKDKC EPLEKQHEKE RKQEEGES.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Orm2 Human
  • View Data Sheet

    Name :

    MAGEA3 Human

    Description:

    Melanoma Antigen Family A, 3 Human Recombinant

    CT1.3, MAGE3, HYPD, Melanoma Antigen family A, 3, MAGE-3 antigen, MAGEA6, Antigen MZ2-D, Melanoma-Associated antigen 3.

    Product # :

    PRO-502

    Price :

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    • description
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    • More Info

    Description

    MAGEA3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a.) and having a molecular mass of 37.1kDa.MAGEA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAGEA3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAGE belongs to the MAGE gene family, that comprises 12 known genes, of which 6 are expressed in tumors. The Melanoma-associated antigen 3 genes were originally isolated from different kinds of tumors, and based on their virtually limited tumor-specific expression in adult tissues, they were used as targets for cancer immunotherapy. MAGEA3 is a tumor-specific antigen extensively expressed in solid and hematologic malignancies, but not in normal tissues, with the exclusion of testis and placenta. Consequently, MAGEA3 is an outstanding candidate tumor antigen.

    • Synonyms

      CT1.3, MAGE3, HYPD, Melanoma Antigen family A, 3, MAGE-3 antigen, MAGEA6, Antigen MZ2-D, Melanoma-Associated antigen 3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMPLEQRS QHCKPEEGLE ARGEALGLVG AQAPATEEQE AASSSSTLVE VTLGEVPAAE SPDPPQSPQG ASSLPTTMNY PLWSQSYEDS SNQEEEGPST FPDLESEFQA ALSRKVAELV HFLLLKYRAR EPVTKAEMLG SVVGNWQYFF PVIFSKASSS LQLVFGIELM EVDPIGHLYI FATCLGLSYD GLLGDNQIMP KAGLLIIVLA IIAREGDCAP EEKIWEELSV LEVFEGREDS ILGDPKKLLT QHFVQENYLE YRQVPGSDPA CYEFLWGPRA LVETSYVKVL HHMVKISGGP HISYPPLHEW VLREGEE

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Magea3 Human
  • View Data Sheet

    Name :

    NRG1 Human

    Description:

    Heregulin-B2 Human Recombinant

    Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.

    Product # :

    CYT-407

    Price :

    Quantity :

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    Shipped at Room temp

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    More Info

    • description
    • source
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    • purity
    • biological activity
    • More Info

    Description

    Recombinant Human Neuregulin-1 beta 2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 61 amino acids and having a total molecular mass of 7.0kDa. NRG-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in PBS, pH 7.4.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using serum free human MCF-7 cells is less than 5ng/ml, corresponding to a specific activity of > 2.0 × 105 U/mg.

    More Info

    • Introduction

      Neuregulin is a signaling protein for ErbB2/ErbB4 receptor heterodimers on the cardiac muscle cells, playing an important role in heart structure and function through inducing ErbB2/ErbB4 receptor phosphorylation and cardiomyocyte differentiation. Research on molecular level discovered that neuregulin recombinant could make disturbed myocardial cell structure into order and strengthen the connection between myocardial cells by intercalated discs re-organization. Pharmacodynamic experiments in animals showed that neuregulin (NRG1) recombinant can reduce the degree of damage on myocardial cells caused by ischemia, hypoxia and viral infection.

    • Synonyms

      Neuregulin-1, NRG1, GGF, HGL, HRGA, NDF, SMDF, HRG, ARIA, GGF2, HRG1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NRG1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Heregulin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NRG1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SHLVKCAEKEKTFCVNGGECFMVKDLSNPSRYLCKCPNEFTGDRCQNYVMASFYKAEELYQ.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Neuregulin Human
  • View Data Sheet

    Name :

    SCGN Human

    Description:

    Secretagogin Human Recombinant

    SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.

    Product # :

    PRO-599

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • More Info

    Description

    SCGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-276 a.a.) and having a molecular mass of 34.2kDa. SCGN is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    SCGN His-Tag (1mg/ml) protein is supplied in 20mM Tris HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
      Secretagogin plays a role in human non-functional pituitary adenomas.

    • Synonyms

      SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, SECRET, DJ501N12.8, Secretagogin.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MDSSREPTLG RLDAAGFWQV WQRFDADEKG YIEEKELDAF FLHMLMKLGT DDTVMKANLH KVKQQFMTTQ DASKDGRIRM KELAGMFLSE DENFLLLFRR ENPLDSSVEF MQIWRKYDAD SSGFISAAEL RNFLRDLFLH HKKAISEAKL EEYTGTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DACSTEERKR DFEKIFAYYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCL GLKINP.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Scgn Human
  • View Data Sheet

    Name :

    UPK3A Human

    Description:

    Uroplakin 3A Human Recombinant

    Uroplakin 3A, UPK3, UPIII, Uroplakin III, UP3A.

    Product # :

    PRO-988

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    UPK3A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 214 amino acids (19-207 a.a.) and having a molecular mass of 23.1kDa.UPK3A is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    UPK3A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 150mM NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      UPK3A is a member of the uroplakin-3 family. Uroplakins (UP) which are transmembrane proteins are important components of the urothelium that pass the lipid bilayer once (UPII, UPIIIa, and UPIIIb) or four times (UPIa and UPIb; both members of the "tetraspanin" family). All hold great luminal/extracellular domains, but only UPIIIa and UPIIIb have significant cytoplasmic shares in their C-termini. UPK3A is an extremely specific and moderately sensitive immunohistochemical marker for primary and metastatic urothelial carcinomas. Alterations in this gene are related to renal adysplasia.

    • Synonyms

      Uroplakin 3A, UPK3, UPIII, Uroplakin III, UP3A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMVNLQP QLASVTFATN NPTLTTVALE KPLCMFDSKE ALTGTHEVYL YVLVDSAISR NASVQDSTNT PLGSTFLQTE GGRTGPYKAV AFDLIPCSDL PSLDAIGDVS KASQILNAYL VRVGANGTCL WDPNFQGLCN PPLSAATEYR FKYVLVNMST GLVEDQTLWS DPIRTNQLTP YSTIDTWPGR RSGG.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Upk3A Human
  • View Data Sheet

    Name :

    Cys-Protein-L

    Description:

    Cys-Protein L Recombinant

    Product # :

    PRO-1933

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    Description

    Recombinant Protein-L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein-L is comprised of 5 IgG-binding regions of protein L (B1-B2-B3-B4-B5) containing 366 amino acids in total and having a molecular mass of 40.6kDa, however, it migrates with an apparent molecular mass of 46kDa on SDS-PAGE. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein-L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-L was lyophilized without any additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Recombinant Protein L is comprised of 5 kappa-binding domains. Protein L has the exceptional ability to bind through kappa light chain interactions without hindering with the antibody’s antigen-binding site. This gives Protein L the capacity to bind a broader range of Ig classes and subclasses than other antibody-binding proteins. The recombinant Protein L is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein L binds to IgG from humans, mice, rats and pigs.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-L should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Protein-L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Cys Protein L
  • View Data Sheet

    Name :

    MIF Human, GST

    Description:

    Macrophage Migration Inhibitor Factor Human Recombinant, GST tag

    Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.

    Product # :

    CYT-401

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    Description

    MIF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-115 a.a) and having a molecular mass of 39.2kDa. MIF is fused to a 230 amino acid GST-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIF protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Macrophage Migration Inhibitory Factor (Glycosylation-Inhibiting Factor), Phenylpyruvate Tautomerase, L-Dopachrome Tautomerase, L-Dopachrome Isomerase, GLIF, MMIF, GIF, Macrophage Migration Inhibitory Factor, Glycosylation-Inhibiting Factor, EC 5.3.3.12, EC 5.3.2.1, Macrophage migration inhibitory factor.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD LVPRGSPEFA MPMFIVNTNV PRASVPDGFL SELTQQLAQA TGKPPQYIAV HVVPDQLMAF GGSSEPCALC SLHSIGKIGG AQNRSYSKLL CGLLAERLRI SPDRVYINYY DMNAANVGWN NSTFA.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mif Human Gst
  • View Data Sheet

    Name :

    LDOC1L Human

    Description:

    Leucine Zipper, Down-Regulated in Cancer 1-Like Human Recombinant

    Protein LDOC1L, Leucine zipper protein down-regulated in cancer cells-like, Mammalian retrotransposon-derived protein 6, LDOC1L, MAR6, MART6, dJ1033E15.2.

    Product # :

    PRO-1153

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    Description

    LDOC1L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-239 a.a) and having a molecular mass of 28.7kDa.LDOC1L is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LDOC1L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% glycerol, 2mM DTT, 0.1mM PMSF and 1mM EDTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leucine zipper down-regulated in cancer 1-like (LDOC1L) is a member of the LDOC1 family. LDOC1L is a nuclear protein containing a leucine zipper-like motif and a proline-rich region that shares noticeable similarity with an SH3-binding domain. LDOC1L localizes to the nucleus and is downregulated in certain cancer cell lines. LDOC1L is believed to regulate the transcriptional response mediated by the nuclear factor kB (NFkB).

    • Synonyms

      Protein LDOC1L, Leucine zipper protein down-regulated in cancer cells-like, Mammalian retrotransposon-derived protein 6, LDOC1L, MAR6, MART6, dJ1033E15.2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMVQPQT SKAESPALAA SPNAQMDDVI DTLTSLRLTN SALRREASTL RAEKANLTNM LESVMAELTL LRTRARIPGA LQITPPISSI TSNGTRPMTT PPTSLPEPFS GDPGRLAGFL MQMDRFMIFQ ASRFPGEAER VAFLVSRLTG EAEKWAIPHM QPDSPLRNNY QGFLAELRRT YKSPLRHARR AQIRKTSASN RAVRERQMLC RQLASAGTGP CPVHPASNGT SPAPALPARA RNL.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ldoc1L Human
  • View Data Sheet

    Name :

    NPPA Human

    Description:

    Natriuretic Peptide A Human Recombinant

    Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND. 

    Product # :

    CYT-1028

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    Description

    NPPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 26-123) containing 106 amino acids including an 8 a.a N-terminal His tag. The total molecular mass is 11.7kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    NPPA filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20 mM Tris buffer, 50 mM NaCl and 5% w/v trehalosa, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Natriuretic Peptide A (NPPA) is a part of the natriuretic peptide family and is involved in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. NPPA is synthesized as a great precursor which releases a peptide from the N-terminus with similarity to vasoactive peptide, cardiodilatin, and another peptide from the C-terminus with natriuretic-diuretic activity. In female pregnancy, NPPA is promoting trophoblast invasion and spiral artery remodeling in uterus.

    • Synonyms

      Natriuretic peptides A, CDD-ANF, Cardiodilatin, CDD, Cardiodilatin-related peptide, CDP, N-terminal proatrial natriuretic peptide, ANP, PND.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. NPPA is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHNP MYNAVSNADL MDFKNLLDHL EEKMPLEDEV VPPQVLSEPN EEAGAALSPL PEVPPWTGEV SPAQRDGGAL GRGPWDSSDR SALLKSKLRA LLTAPR.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nppa Human
  • View Data Sheet

    Name :

    PCOLCE Human

    Description:

    Procollagen C-Endopeptidase Enhancer Human Recombinant

    Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 1.

    Product # :

    ENZ-863

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    Description

    PCOLCE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (26-449 a.a) and having a molecular mass of 47.9kDa. PCOLCE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PCOLCE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.

    • Synonyms

      Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQD.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Pcolce Human
  • View Data Sheet

    Name :

    MMP 9 Human

    Description:

    Matrix Metalloproteinase-9 Human Recombinant

    Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    Product # :

    ENZ-438

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    Description

    MMP-9 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 338 amino acids fragment (113-450) corresponding to the catalytic domain of the protein, having a total molecular mass of 42.03kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The MMP-9 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MMP-9 protein is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. MMP9 can also degrade fibronectin but not laminin or Pz-peptide.
      MMP9 defects may be a cause of susceptibility to intervertebral disc disease (IDD), also known as lumbar disk herniation (LDH).

    • Synonyms

      Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      4.5kDa His Tag-DLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDAD
      IVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFP
      FIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTRDGNADGKPCQFPFIFQGQSYSA
      CTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDG
      RLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVN
      GIRHLYGP.

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    Mmp 9 Human
  • View Data Sheet

    Name :

    Collagen-III Bovine

    Description:

    Bovine Collagen-III

    Product # :

    PRO-2731

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    Description

    Mouse Collagen-III is a natural protein purified from washed dissected tissue into dilute acetic acid. Collagen-I is purified by proprietary chromatographic techniques.

    Source

    Bovine washed dissected tissue.

    Formulation

    Collagen-III was lyophilized without additives.

    Purity

    > 90.0%.

    More Info

    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Collagen-III although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-III should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to add 20 mM acetic acid to prepare a working stock solution of 1-5 mg/ml, which can then be further diluted to other aqueous solutions. Suspension should be shaken or stirred for several hours or overnight between 2-8°C.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Collagen Iii Bovine
  • View Data Sheet

    Name :

    MMP12 Human (1-33)

    Description:

    Matrix Metalloproteinase 12 (1-33 a.a.) Human Recombinant

    Product # :

    ENZ-1201

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    Description

    The MMP12 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MMP12 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 33 amino acid residues of the MMP12 Human, 1-33 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized MMP12 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Amino Acid Sequence

      MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFG.

    • Background

      Matrix Metalloproteinase 12 also known as MMP12 is 1 of the main enzymes in the MMP family which is primarily produced by macrophages and neutrophils. MMP12 is implicated in the breakdown of elastin and in the development of chronic inflammatory diseases, such as emphysema, COPD and atherosclerosis. MMP12 is upregulated and contributes to tissue remodeling in inflammatory responses which is essential for wound healing and immune defense. MMP12 catalyzes the cleavage of collagen, elastin and other ECM components. Its activity is regulated in normal tissues to avoid pathological degradation.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mmp12 Enzyme
  • View Data Sheet

    Name :

    NDRG1 Human

    Description:

    N-Myc Downstream Regulated 1 Human Recombinant

    Protein NDRG1, N-myc downstream-regulated gene 1 protein, Differentiation-related gene 1 protein, Reducing agents and tunicamycin-responsive protein, Nickel-specific induction protein Cap43, DRG-1, RTP, Rit42, NDRG1, CAP43, DRG1, GC4, NDR1, NMSL, TDD5, CMT4D, HMSNL, TARG1, PROXY1.

    Product # :

    PRO-724

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    • More Info

    Description

    NDRG1 Human Recombinant fused with 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 402 amino acids (1-394 a.a.) and having a molecular mass of 43.9 kDa.The NDRG1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDRG1 solution contains 20mM Tris-HCl buffer (pH8.0), 0.1mM PMSF and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using MCF7 cell. The ED50 for this effect is 0.5 - 1.5ng/ml, corresponding to a Specific Activity of 666,000 -2,000,000 IU/mg.

    More Info

    • Introduction

      NDRG1 is a cytoplasmic protein that is involved in stress responses, hormone responses, cell growth, and differentiation. NDRG1 is one of 4 members of the NDRG ?/?-hydrolase family. NDRG1 is classified in databases as a tumor suppressor and heavy metal-response protein. NDRG1’s functions include cell-cycle regulation, cellular differentiation, apoptosis, hypoxia response and metal-ion sensing. NDRG1 is also essential for p53-mediated caspase activation and apoptosis. The NDRG1 is a Rab4a effector that is involved in vesicular recycling of E-cadherin. NDRG1 is ubiquitous; it is expressed most notably in placental membranes and prostate, kidney, small intestine, and ovary tissues. NDRG1 has reduced expression in adenocarcinomas compared to normal tissues.
      NDRG1 gene mutations are reported to be the cause for hereditary motor and sensory neuropathy-Lom (HMSNL), which is a severe autosomal recessive form of Charcot- Marie-Tooth (CMT) disease. In addition, decreased NDRG1 expression in glioma is linked to tumor progression. On the other hand, overexpression of NDRG1 is connected to malignant status of esophageal cancer. NDRG1 may also have a role in portal vein invasion and intrahepatic metastasis in human hepatocellular carcinoma.

    • Synonyms

      Protein NDRG1, N-myc downstream-regulated gene 1 protein, Differentiation-related gene 1 protein, Reducing agents and tunicamycin-responsive protein, Nickel-specific induction protein Cap43, DRG-1, RTP, Rit42, NDRG1, CAP43, DRG1, GC4, NDR1, NMSL, TDD5, CMT4D, HMSNL, TARG1, PROXY1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MSREMQDVDL AEVKPLVEKG ETITGLLQEF DVQEQDIETL HGSVHVTLCG TPKGNRPVIL TYHDIGMNHK TCYNPLFNYE DMQEITQHFA
      VCHVDAPGQQ DGAASFPAGY MYPSMDQLAE MLPGVLQQFG LKSIIGMGTG AGAYILTRFA LNNPEMVEGL VLINVNPCAE GWMDWAASKI SGWTQALPDM VVSHLFGKEE MQSNVEVVHT YRQHIVNDMN PGNLHLFINA YNSRRDLEIE RPMPGTHTVT LQCPALLVVG DSSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLDGT RSRSHTSEGT RSRSHTSEGT RSRSHTSEGA HLDITPNSGA AGNSAGPKSM EVSCLEHHHH HH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ndrg1 Human
  • View Data Sheet

    Name :

    BD 1 Human

    Description:

    Beta Defensin-1 Human Recombinant

    Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

    Product # :

    CYT-564

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    Description

    Beta Defensin-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 47 amino acids and having a molecular mass of 5 kDa.The BD-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Human BD-1 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM sodium chloride.

    Purity

    Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

    More Info

    • Synonyms

      Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Beta Defensin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Beta Defensin-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.

    • Background

      Beta Defensin-1 Human Recombinant: Unveiling its Potential in Innate Immunity and Therapeutic Applications

      Abstract:


      Beta Defensin-1 (BD-1), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-1 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-1 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-1, highlighting its impact on innate immunity and its therapeutic potential.

      Introduction:


      Innate immunity serves as the first line of defense against invading pathogens. BD-1, a key peptide within the defensin family, exhibits broad-spectrum antimicrobial activity and plays a pivotal role in host defense mechanisms. This paper provides an overview of BD-1, shedding light on its structure, function, and therapeutic potential.

      BD-1 Structure and Function:


      BD-1 is a cationic peptide with a conserved cysteine motif that confers its antimicrobial properties. It acts by disrupting the integrity of microbial cell membranes, leading to microbial death. Additionally, BD-1 exhibits immunomodulatory effects by stimulating immune cell recruitment and cytokine production.

      Antimicrobial Properties and Therapeutic Applications:


      BD-1 demonstrates antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Its ability to combat multidrug-resistant strains makes it an attractive candidate for the development of novel antimicrobial therapies. Furthermore, BD-1's immunomodulatory effects contribute to its potential in treating inflammatory and infectious diseases.

      Therapeutic Potential of BD-1 Human Recombinant:


      BD-1 human recombinant holds significant promise in the field of immunotherapy. Strategies aimed at enhancing BD-1 expression or delivering exogenous BD-1 may help boost innate immune responses in patients with compromised immune systems or chronic infections. Furthermore, BD-1-based therapeutics could be developed to combat antibiotic-resistant infections and prevent biofilm formation.

      Challenges and Future Directions:


      While BD-1 shows immense therapeutic potential, challenges must be addressed. Further research is necessary to optimize the delivery methods of BD-1 and evaluate its long-term safety and efficacy. Additionally, understanding the interplay between BD-1 and other immune factors will aid in developing combinatorial approaches for enhanced therapeutic outcomes.

      Conclusion:


      BD-1 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-1 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize the field of immunotherapy and improve patient outcomes.

      What is the molecular weight/Mw of BD1 Protein?
      BD1 Protein has a total Mw of 5kDa.

      What is the source or expression system of BD1 Protein?
      Escherichia Coli.

      What is the Purity of BD1 Protein?
      BD1 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD1 Protein?
      Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

      What is the amino acid sequence of BD1 Protein?
      GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.

      What applications can BD1 Protein be used in?
      BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD1 Protein?
      The endotoxin level is minimal, BD1 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Beta Defensin 1 Human
  • View Data Sheet

    Name :

    CAPG Human

    Description:

    Capping Protein Gelsolin-Like Human Recombinant

    AFCP, CAPG, Macrophage-capping protein, Actin regulatory protein CAP-G, MCP.

    Product # :

    PRO-759

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    Description

    CAPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-348 a.a.) and having a molecular mass of 38.5 kDa. The CAPG protein is purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris buffer pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CAPG is part of the gelsolin/villin family of actin-regulatory proteins. CAPG reversibly blocks the barbed ends of F-actin filaments in a Ca2+ and phosphoinositide-regulated method, though it does not separate preformed actin filaments. By capping the barbed ends of actin filaments, CAPG contributes to the control of actin-based motility in non-muscle cells. CAPG is involved in macrophage function. CAPG is involved in regulating cytoplasmic and/or nuclear structures via possible interactions with actin. CAPG binds DNA. CAPG lacks a nuclear export sequence present in structurally related proteins. CAPG is a tumor suppressor protein that plays a role in the tumorigenic progression of certain cancers. Dysregulated expression of CAPG was found in premalignant and malignant oral carcinogenesis.

    • Synonyms

      AFCP, CAPG, Macrophage-capping protein, Actin regulatory protein CAP-G, MCP.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MYTAIPQSGS PFPGSVQDPG LHVWRVEKLK PVPVAQENQG VFFSGDSYLV LHNGPEEVSH LHLWIGQQSS RDEQGACAVL AVHLNTLLGE RPVQHREVQG NESDLFMSYF PRGLKYQEGG VESAFHKTST GAPAAIKKLY QVKGKKNIRA TERALNWDSF NTGDCFILDL GQNIFAWCGG KSNILERNKA RDLALAIRDS ERQGKAQVEI VTDGEEPAEM IQVLGPKPAL KEGNPEEDLT ADKANAQAAA LYKVSDATGQ MNLTKVADSS PFALELLISD DCFVLDNGLC GKIYIWKGRK ANEKERQAAL QVAEGFISRM QYAPNTQVEI LPQGRESPIF KQFFKDWK.

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    Capg Human
  • View Data Sheet

    Name :

    SERPINA5 Human, Active

    Description:

    Serpin Peptidase Inhibitor, Clade A Member 5 Human Recombinant, Active

    Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.

    Product # :

    PRO-2523

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    Description

    SERPINA5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (20-406 a.a) and having a molecular mass of 45.9kDa.SERPINA5 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SERPINA5 protein solution (0.5mg/ml) contains 150mM NaCl, 10% glycerol & 20 mM MES buffer (pH6.0).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit Thrombin cleavage of substrate Boc-VPR-AMC. The IC50 for this effect is less or equal to 2 nM.

    More Info

    • Introduction

      SERPINA5 up regulates TAFI activation by inhibiting the protein C activation. SERPINA5 is a significant regulator in the equilibrium between coagulation and fibrinolysis by differentially inhibiting the activation of TAFI and of Protein-C. SERPINA5 belongs to the serpin serine proteinase inhibitor family. SERPINA5 protein inhibits plasminogen activators as well as activated protein C.
      SERPINA5 is secreted in plasma & liver. SERPINA5 is involved in cell inflammation, proliferation, apoptosis, tumour cell migration, invasion, and metastasis. Moreover, SERPINA5 controls the invasive potential of renal cell carcinoma by inhibiting urinary plasminogen activator secreted by the cells. SERPINA5 participtes in regulating key serine proteases which are involved in metastatic prostate disease.

    • Synonyms

      Serpin Family A Member 5, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 5, Acrosomal Serine Protease Inhibitor 3 4 Protein C Inhibitor, PLANH3, PAI-3, PROCI, PAI3, PCI, Plasminogen Activator Inhibitor III, Plasminogen Activator Inhibitor-3, Plasminogen Activator Inhibitor 3, Plasma Serine Protease Inhibitor, Serpin A5, PCI-B.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MHRHHPREMK KRVEDLHVGA TVAPSSRRDF TFDLYRALAS AAPSQNIFFS PVSISMSLAM LSLGAGSSTK MQILEGLGLN LQKSSEKELH RGFQQLLQEL NQPRDGFQLS LGNALFTDLV VDLQDTFVSA MKTLYLADTF PTNFRDSAGA MKQINDYVAK QTKGKIVDLL KNLDSNAVVI MVNYIFFKAK WETSFNHKGT QEQDFYVTSE TVVRVPMMSR EDQYHYLLDR NLSCRVVGVP YQGNATALFI LPSEGKMQQV ENGLSEKTLR KWLKMFKKRQ LELYLPKFSI EGSYQLEKVL PSLGISNVFT SHADLSGISN HSNIQVSEMV HKAVVEVDES GTRAAAATGT IFTFRSARLN SQRLVFNRPF LMFIVDNNIL FLGKVNRP.

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    Serpina5 Protein
  • View Data Sheet

    Name :

    NFKBIB Human

    Description:

    NF-kappa-B Inhibitor Beta Human Recombinant

    NF-kappa-B inhibitor beta, NF-kappa-BIB, I-kappa-B-beta, IkB-B, IkB-beta, IkappaBbeta, Thyroid receptor-interacting protein 9, TR-interacting protein 9, TRIP-9, NFKBIB, IKBB, TRIP9.

    Product # :

    PRO-1046

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    Description

    NFKBIB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (1-356 a.a) and having a molecular mass of 40.3kDa (Molecular weight on SDS-PAGE will appear higher).NFKBIB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NFKBIB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NF-kappa-B inhibitor beta (NFKBIB) is a member of the NF-kappa-B inhibitor family, which inhibit NF-kappa-B by complexing with, and trapping it in the cytoplasm. Phosphorylation of serine residues on these proteins by kinases marks them for destruction via the ubiquitination pathway, thus allowing activation of the NF-kappa-B, which translocates to the nucleus to act as a transcription factor.

    • Synonyms

      NF-kappa-B inhibitor beta, NF-kappa-BIB, I-kappa-B-beta, IkB-B, IkB-beta, IkappaBbeta, Thyroid receptor-interacting protein 9, TR-interacting protein 9, TRIP-9, NFKBIB, IKBB, TRIP9.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMAGVAC LGKAADADEW CDSGLGSLGP DAAAPGGPGL GAELGPGLSW APLVFGYVTE DGDTALHLAV IHQHEPFLDF LLGFSAGTEY MDLQNDLGQT ALHLAAILGE TSTVEKLYAA GAGLCVAERR GHTALHLACR VGAHACARAL LQPRPRRPRE
      APDTYLAQGP DRTPDTNHTP VALYPDSDLE KEEEESEEDW KLQLEAENYE GHTPLHVAVI HKDVEMVRLL RDAGADLDKP EPTCGRSPLH LAVEAQAADV LELLLRAGAN PAARMYGGRT PLGSAMLRPN PILARLLRAH GAPEPEGEDE KSGPCSSSSD SDSGDEGDEY DDIVVHSSRS QTRLPPTPAS KPLPDDPRPV.

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    Nfkbib Human
  • View Data Sheet

    Name :

    CCL13 Human

    Description:

    Monocyte Chemotactic Protein-4 Human Recombinant (CCL13)

    Small inducible cytokine A13, CCL13, Monocyte chemotactic protein 4, MCP-4, Monocyte chemoattractant protein 4, CK-beta-10, NCC-1, chemokine (C-C motif) ligand 13, NCC1, CKb10, SCYL1, SCYA13, MGC17134.

    Product # :

    CHM-319

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    Description

    Monocyte Chemotactic Protein-4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 75 amino acids and having a molecular mass of 8.6 kDa. The MCP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution in 20mM PB, pH 7.4, 130mM NaCl.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the ability of MCP-4 to chemoattaract human monocytes at 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 13 (CCL13 / MCP-4) is a small cytokine belonging to the CC chemokine family. The MCP-4 gene is located on human chromosome 17 within a large cluster of other CC chemokines. MCP-4 induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. Activity of the MCP-4 chemokine has been implicated in allergic reactions such as asthma. MCP-4 can be induced by the inflammatory cytokines interleukin-1 and TNF-a.

    • Synonyms

      Small inducible cytokine A13, CCL13, Monocyte chemotactic protein 4, MCP-4, Monocyte chemoattractant protein 4, CK-beta-10, NCC-1, chemokine (C-C motif) ligand 13, NCC1, CKb10, SCYL1, SCYA13, MGC17134.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCP-4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized MCP-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPDALNVPSTCCFTFSSKKISLQRLKSYVITTSRCPQKAV
      IFRTKLGKEICADPKEKWVQNYMKHLGRKAHTLKT.

    • Background

      What is the molecular weight/Mw of CCL13 HUMAN Protein?
      CCL13 HUMAN Protein has a total Mw of 8.6kDa.

      What is the source or expression system of CCL13 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL13 HUMAN Protein?
      CCL13 HUMAN Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL13 HUMAN Protein?
      The specific activity as determined by the ability of MCP-4 to chemoattaract human monocytes at 10-100ng/ml, corresponding to a Specific Activity of 10,000-100,000 units/mg.

      What is the amino acid sequence of CCL13 HUMAN Protein?
      QPDALNVPSTCCFTFSSKKISLQRLKSYVITTSRCPQKAV
      IFRTKLGKEICADPKEKWVQNYMKHLGRKAHTLKT.

      What applications can CCL13 HUMAN Protein be used in?
      CCL13 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL13 HUMAN Protein?
      The endotoxin level is minimal, CCL13 HUMAN Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mcp 4 Human
  • View Data Sheet

    Name :

    Dengue Envelope-3 45kDa

    Description:

    Dengue Virus Subtype 3 Envelope 45kDa Recombinant

    Product # :

    DEN-023

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    Description

    Recombinant Dengue Virus Subtype 3 Envelope 45kDa (a.a 43-413) is produced in E.coli. This protein is fused to 6xHis tag at C-terminus.

    Source

    E.coli.

    Formulation

    25mM Tris base and 10mM K2CO3.

    Purity

    Protein is >95% pure as determined by 10% SDS-PAGE (coomassie staining).

    More Info

    • Introduction

      Dengue fever is affected by 1 of 4 closely linked virus serotypes of the genus Flavivirus, family Flaviviridae. One might have dengue fever infected by the different serotype virus after the primary infection. Detection of particular antibodies to dengue viruses is used for the diagnosis in clinic. Recently, lateral flow rapid test products have become a most suitable and known method in the clinical diagnosis. Though, there is difficulty for manufacturers to have the dengue antigens with a whole coverage for Dengue IgG & IgM recognition for all 4 serotype infections as well as with colloid gold binding ability. 8 dengue antigens have been established for the lateral flow products which are well defined for their coverage of dengue IgG & IgM recognition. The researcher can select the products below based on their own specific application.

    • Stability

      Dengue Envelope-3 45kDa although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Immunoassay.

    • Purification Method

      Purified by proprietary chromatographic technique.

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    Dengue Envelope 3 45Kda
  • View Data Sheet

    Name :

    GH Antagonist Ovine

    Description:

    Growth Hormone Antagonist Ovine Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-215

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    Description

    Somatotropin Ovine Antagonist Recombinant G119R produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids and having a molecular mass of 22 kDa. The Somatotropin Ovine Antagonist Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045M NaHCO3, pH 9.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC
    (b) Analysis by Gel Filtration. (c) Analysis by SDS-PAGE.

    Biological Activity

    GH G119R acts as antagonist using an in vitro bioassay in PDF-P1 3B9 cells stably transfected with rabbit GH receptors. It is capable of forming a 1:1 complex with the recombinant ovine growth hormone receptor extracellular domain (ECD) and binds to this ECD with affinity similar the the wild type oGH.

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GH G119R although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GH G119R in 0.4% NaHCO3 or water adjusted to pH 9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Phe-Pro-Ala.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.63 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

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    Gh Antagonist Ovine
  • View Data Sheet

    Name :

    OmpA S.Enteritidis

    Description:

    Salmonella Enteritidis Outer Membrane Protein-A Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-1918

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    Description

    The Recombinant Salmonella Enteritidis Outer Membrane Protein A, E.Coli derived, 330 amino acids, contains the ompA immunodominant regions. The protein is fused to a His tag at C-terminal and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    PBS and 25MmM Arginine.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      OmpA S.Enteritidis Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Immunoassay. Outer membrane protein A (ompA) of S. Enteritidis is a protein directly exposing to outsides of this organism, In hens, the production of antibodies against outer membrane protein A (ompA) during the infection has been demonstrated by inoculating both the complete bacterium and expressed protein produced from ompA DNA vaccine. Vaccination by ompA protein to hens is a poteintail tool to control S. enteritidis contaminated eggs into market, and prevent human foodborne disease from eggs.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ompa Senteritidis
  • View Data Sheet

    Name :

    Collagen-IV Bovine

    Description:

    Bovine Collagen-IV

    Product # :

    PRO-2678

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Bovine Collagen-IV is a natural protein purified from bovine placenta. Collagen-IV is purified by proprietary chromatographic techniques.

    Source

    Bovine placenta.

    Formulation

    Collagen-IV was lyophilized without additives.

    Purity

    > 90.0% .

    More Info

    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Collagen-IV although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-IV should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Collagen-IV in 20 mM acetic acid not less than 1mg/ml, which can then be further diluted to other aqueous solutions.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Collagen Iv Bovine
  • View Data Sheet

    Name :

    Y.Enterocolitica (O:9) YopB

    Description:

    Yersinia Enterocolitica (O:9) YopB Recombinant

    Protein YopD, pYV0054.

    Product # :

    PRO-2575

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Recombinant Yersinia Enterocolitica (O:9) YopB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain having a calculated molecular mass of 43kDa. Y.Enterocolitica (O:9) YopB is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Y.Enterocolitica (O:9) YopB is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gastroenteritis which has been identified as caused by Yersinia Enterocolitica has been discovered by virulent isolates of the bacteria. During infection, pores are being formed in the presence of adapter protein Yersiniosis. YopB's Interaction with the target membrane to form pores enables the entrance of YopE effectors to the cytoplasmic space of the host’s cell.

    • Synonyms

      Protein YopD, pYV0054.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Immunological Activity

      1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with positive/negative samples.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Yopb Protein
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